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Science 26 July 1991:
Vol. 253. no. 5018, pp. 445 - 448
DOI: 10.1126/science.1862345
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Articles
Science, Vol 253, Issue 5018, 445-448
Copyright © 1991 by American Association for the Advancement of Science
Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist
M Adler,
RA Lazarus,
MS Dennis,
and
G Wagner
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
The structure of kistrin, which is a member of a homologous family of glycoprotein IIb-IIIa (GP IIb-IIIa) antagonists and potent protein inhibitors of platelet aggregation, has been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The 68-residue protein consists of a series of tightly packed loops held together by six disulfide bonds and has almost no regular secondary structure. Kistrin has an Arg-Gly-Asp (RGD) adhesion site recognition sequence important for binding to GP IIb-IIIa that is located at the apex of a long loop across the surface of the protein.
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